4RR2

Crystal structure of human primase

4RR2 の概要

• エントリーDOI: 10.2210/pdb4rr2/pdb
• 分子名称: DNA primase small subunit, DNA primase large subunit, ZINC ION, ... (5 entities in total)
• 機能のキーワード: pol alpha, primase, dna replication, polymerase, iron-sulfur cluster, dna-binding, dna-directed rna polymerase, metal-binding, nucleotidyltransferase, phosphoprotein, primosome, transferase
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 218226.32

構造登録者

Baranovskiy, A.G.,Gu, J.,Suwa, Y.,Babayeva, N.D.,Tahirov, T.H. (登録日: 2014-11-05, 公開日: 2015-01-21, 最終更新日: 2024-02-28)

主引用文献

Baranovskiy, A.G.,Zhang, Y.,Suwa, Y.,Babayeva, N.D.,Gu, J.,Pavlov, Y.I.,Tahirov, T.H.
Crystal structure of the human primase.
J.Biol.Chem., 290:5635-5646, 2015

PubMed Abstract: DNA replication in bacteria and eukaryotes requires the activity of DNA primase, a DNA-dependent RNA polymerase that lays short RNA primers for DNA polymerases. Eukaryotic and archaeal primases are heterodimers consisting of small catalytic and large accessory subunits, both of which are necessary for RNA primer synthesis. Understanding of RNA synthesis priming in eukaryotes is currently limited due to the lack of crystal structures of the full-length primase and its complexes with substrates in initiation and elongation states. Here we report the crystal structure of the full-length human primase, revealing the precise overall organization of the enzyme, the relative positions of its functional domains, and the mode of its interaction with modeled DNA and RNA. The structure indicates that the dramatic conformational changes in primase are necessary to accomplish the initiation and then elongation of RNA synthesis. The presence of a long linker between the N- and C-terminal domains of p58 provides the structural basis for the bulk of enzyme's conformational flexibility. Deletion of most of this linker affected the initiation and elongation steps of the primer synthesis.

PubMed: 25550159
DOI: 10.1074/jbc.M114.624742

実験手法

X-RAY DIFFRACTION (2.65 Å)